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Database: UniProt
Entry: A0A0N0T8K4_9NOCA
LinkDB: A0A0N0T8K4_9NOCA
Original site: A0A0N0T8K4_9NOCA 
ID   A0A0N0T8K4_9NOCA        Unreviewed;       859 AA.
AC   A0A0N0T8K4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   12-SEP-2018, entry version 14.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=ADL03_21800 {ECO:0000313|EMBL:KOV83178.1};
OS   Nocardia sp. NRRL S-836.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=1519492 {ECO:0000313|EMBL:KOV83178.1, ECO:0000313|Proteomes:UP000037746};
RN   [1] {ECO:0000313|EMBL:KOV83178.1, ECO:0000313|Proteomes:UP000037746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL S-836 {ECO:0000313|EMBL:KOV83178.1,
RC   ECO:0000313|Proteomes:UP000037746};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-glucosidic
CC       linkages in cellulose, lichenin and cereal beta-D-glucans.
CC       {ECO:0000256|RuleBase:RU361166}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E)
CC       family. {ECO:0000256|RuleBase:RU361166}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KOV83178.1}.
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DR   EMBL; LGDY01000102; KOV83178.1; -; Genomic_DNA.
DR   RefSeq; WP_053735329.1; NZ_LGDY01000102.1.
DR   EnsemblBacteria; KOV83178; KOV83178; ADL03_21800.
DR   PATRIC; fig|1519492.3.peg.4683; -.
DR   Proteomes; UP000037746; Unassembled WGS sequence.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02850; E_set_Cellulase_N; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.120.260; -; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR004197; Cellulase_Ig-like.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF02927; CelD_N; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00698; GLYCOSYL_HYDROL_F9_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361166};
KW   Cellulose degradation {ECO:0000256|RuleBase:RU361166};
KW   Complete proteome {ECO:0000313|Proteomes:UP000037746};
KW   Glycosidase {ECO:0000256|RuleBase:RU361166};
KW   Hydrolase {ECO:0000256|RuleBase:RU361166};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361166};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037746};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL        1     30       {ECO:0000256|RuleBase:RU361166}.
FT   CHAIN        31    859       Endoglucanase. {ECO:0000256|RuleBase:
FT                                RU361166}.
FT                                /FTId=PRO_5005732772.
FT   DOMAIN      752    859       CBM2. {ECO:0000259|PROSITE:PS51173}.
FT   ACT_SITE    720    720       {ECO:0000256|PROSITE-ProRule:PRU10060}.
FT   ACT_SITE    729    729       {ECO:0000256|PROSITE-ProRule:PRU10060}.
SQ   SEQUENCE   859 AA;  90085 MW;  06FC3E9220A84503 CRC64;
     MRSQPPRLLA AALLTALAAT AIPAAGTAEA AEYERVLNGK FDSGSADPWW SSAGVTNRIT
     GGELCASVTG GTTNPWDALV GQNGVPFESG QSYTLSFDAH ATTAQPVAAA AGESVSPYRG
     IARQEFAVTP TKQHFTFSFT STLDFPDAGN GQVAFQLGGQ TADNTICVDN VSLVGGVKPP
     GGVVPNPTRK VQVDQVGYVP GLPKRATLVS TATTPQTWTL KNSAGATVAS GQSTPKGADA
     TSGDSVHSID FSSFDTPGTG YTLVVGTDSS FPFDISADVV KKLRYDALAF FYHQRSGTPI
     EAQYVGDQYA RPAGHINVAP NQGDNNVPCR ADLACGYTLD VRGGWYDAGD HGKYVVNGGI
     SAWQLLNSYE RAARIGDASA FRDGTLAIPE KANGVPDLLD EARWEVDFLL KMQAPDGMAH
     HKVHDANWTA LPTRPELDDQ PRRLSATSTA ATLNLAAVAA QASRLWKSVD ATYSAKLLTA
     ARKAYAAAKA NPNKIADPND GTGGGAYSDN TVSDEFYWAA AELYATTGES AYGTDVTSSP
     HYKAASLTRA GFYWGGTAPL GDITLALVPT GLPAADVTAI KTAFATVADQ HLAAMAQMGY
     ATPYDNSVDG YVWGSNSAVL NNAQVLALAH DFTGADKYRD GVFEALHYLL GRNPLSTSYV
     AGYGEQAVQN VHHRFWAKQN DPTLPIAPPG SLSGGPNSGL QDPIVQRLLP GCPQQKCWVD
     DIGAYSVNEV AVNWNSALAW VSGWAAEKSG KPPVPVADCE VTFTANRWSS GLSANVAVKN
     TGTTAWTSWK LGFALPGTQQ VTAGWSANWS QTGRDVTATN MSWNGKVEAG KSVYIGFNAS
     GAGGDPTAFT INGKSCKTG
//
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